메뉴 건너뛰기




Volumn 6, Issue 6, 1996, Pages 744-756

The relationship between structure and function for the sulfite reductases

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; BACTERIAL ENZYME; HEMOPROTEIN; IRON SULFUR PROTEIN; NITRITE; NITRITE REDUCTASE; SULFIDE; SULFITE; SULFITE REDUCTASE;

EID: 0030472457     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80003-0     Document Type: Article
Times cited : (133)

References (93)
  • 1
    • 0039399893 scopus 로고
    • Biochemistry of the sulfur cycle
    • Edited by Greenberg DM. New York: Academic Press
    • 1. Siegel LM: Biochemistry of the sulfur cycle. In Metabolic Pathways, vol 7. Edited by Greenberg DM. New York: Academic Press; 1975.
    • (1975) Metabolic Pathways , vol.7
    • Siegel, L.M.1
  • 3
    • 0004080075 scopus 로고
    • Cambridge: Cambridge University Press
    • 3. Postgate JR (Ed):The Sulfate-Reducing Bacteria. Cambridge: Cambridge University Press; 1979.
    • (1979) The Sulfate-reducing Bacteria
  • 5
    • 0028672437 scopus 로고
    • Enzymology and molecular biology of sulfate reduction in extremely thermophilic archaeon archaeoglobus fulgidus
    • 5. Dahl C, Speich N, Trüper HG: Enzymology and molecular biology of sulfate reduction in extremely thermophilic archaeon Archaeoglobus fulgidus. Methods Enzymol 1994, 243:331-349.
    • (1994) Methods Enzymol , vol.243 , pp. 331-349
    • Dahl, C.1    Speich, N.2    Trüper, H.G.3
  • 7
    • 0015212057 scopus 로고
    • Purification of the enzyme reducing bisulfite to trithionate from Desulfovibrio vulgaris and its identification as Desulfoviridin
    • 7. Lee J, Peck HD Jr: Purification of the enzyme reducing bisulfite to trithionate from Desulfovibrio vulgaris and its identification as Desulfoviridin. Biochem Biophys Res Commun 1971, 45:583-589.
    • (1971) Biochem Biophys Res Commun , vol.45 , pp. 583-589
    • Lee, J.1    Peck H.D., Jr.2
  • 8
    • 0015881957 scopus 로고
    • Isolation of a new pigment desulforubidin from Desulfovibrio desulfuricans (Norway strain) and its role in sulfite reduction
    • 8. Lee J, Yi C, LeGall J, Peck HD Jr: Isolation of a new pigment desulforubidin from Desulfovibrio desulfuricans (Norway Strain) and its role in sulfite reduction J Bacteriol 1973, 115:453-455.
    • (1973) J Bacteriol , vol.115 , pp. 453-455
    • Lee, J.1    Yi, C.2    LeGall, J.3    Peck H.D., Jr.4
  • 9
    • 0015694449 scopus 로고
    • Isolation of assimilatory- and dissimilatory-type sulfite reductases from Desulfovibrio vulgaris
    • 9. Lee J, LeGall J, Peck HD Jr: Isolation of assimilatory- and dissimilatory-type sulfite reductases from Desulfovibrio vulgaris. J Bacteriol 1973, 115:529-543.
    • (1973) J Bacteriol , vol.115 , pp. 529-543
    • Lee, J.1    LeGall, J.2    Peck H.D., Jr.3
  • 10
    • 0015411507 scopus 로고
    • Biochemical studies on sulfate-reducing bacteria. XI. Purification and some properties of desulfoviridin
    • 10. Kobayashi K, Takahasi E, Ishimoto M: Biochemical studies on sulfate-reducing bacteria. XI. Purification and some properties of desulfoviridin. J Biochem (Tokyo) 1972, 72:879-887.
    • (1972) J Biochem (Tokyo) , vol.72 , pp. 879-887
    • Kobayashi, K.1    Takahasi, E.2    Ishimoto, M.3
  • 11
    • 0019644241 scopus 로고
    • Siroheme as an active catalyst in sulfite reduction
    • 11. Seki Y, Sogawa N, Ishimoto M: Siroheme as an active catalyst in sulfite reduction. J Biochem (Tokyo) 1981, 90:1487-1492.
    • (1981) J Biochem (Tokyo) , vol.90 , pp. 1487-1492
    • Seki, Y.1    Sogawa, N.2    Ishimoto, M.3
  • 12
    • 0011309053 scopus 로고
    • Characterization of a new type of dissimilatory sulfite reductase present in Thermodesulfobacterium commune
    • 12. Halchikian EC, Zeikus JG: Characterization of a new type of dissimilatory sulfite reductase present in Thermodesulfobacterium commune. J Bacteriol 1983, 223:79-80.
    • (1983) J Bacteriol , vol.223 , pp. 79-80
    • Halchikian, E.C.1    Zeikus, J.G.2
  • 14
    • 0011271239 scopus 로고
    • Physiology, biochemistry, and genetics of nitrite reduction by Escherichia coli
    • Edited by Wray JL, Kinghorn JR. Oxford; Oxford Science Publications
    • 14. Cole JA: Physiology, biochemistry, and genetics of nitrite reduction by Escherichia coli. In Molecular and Genetic Aspects of Nitrate Assimilation. Edited by Wray JL, Kinghorn JR. Oxford; Oxford Science Publications; 1989:229-243.
    • (1989) Molecular and Genetic Aspects of Nitrate Assimilation , pp. 229-243
    • Cole, J.A.1
  • 15
    • 0028809514 scopus 로고
    • Sulfite reductase at 1.6Å: Evolution and catalysis for the reductions of inorganic anions
    • 15. Crane BR, Siegel LM, Getzoff ED: Sulfite reductase at 1.6Å: evolution and catalysis for the reductions of inorganic anions. Science 1995, 270:59-67. The three-dimensional structures of E. coli SiRHP in complex with phosphate and sulfite reveal the active center and cofactor assembly for this class of enzyme, and allow a structural basis for interpreting the catalytic mechanism. A previously unrecognized twofold symmetry within the SiRHP polypeptide is potentially relevant to evolutionary development and conservation of structure among the SiRs and NiRs.
    • (1995) Science , vol.270 , pp. 59-67
    • Crane, B.R.1    Siegel, L.M.2    Getzoff, E.D.3
  • 16
    • 0028869891 scopus 로고
    • Conservation of the genes for dissimilatory sulfite reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by PCR
    • 16. Karkhoff-Schweizer RR, Huber DPW, Voordouw G: Conservation of the genes for dissimilatory sulfite reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by PCR. Appl Environ Microbiol 1995, 61:290-296. The sequences for the α and β subunits of desulfoviridin from the mesophilic sulfate-reducing bacteria D. vulgaris are compared with those from the thermophilic archeon A. fulgidus and found to be quite homologous.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 290-296
    • Karkhoff-Schweizer, R.R.1    Huber, D.P.W.2    Voordouw, G.3
  • 17
    • 0027275049 scopus 로고
    • Dissimilatory sulfite reductase from archaeoglobus fulgidus: Physicochemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes
    • 17. Dahl C, Kredich NM, Deutzmann R, Trüper HG: Dissimilatory sulfite reductase from Archaeoglobus fulgidus: physicochemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes. J Gen Microbiol 1993, 139:1817-1828.
    • (1993) J Gen Microbiol , vol.139 , pp. 1817-1828
    • Dahl, C.1    Kredich, N.M.2    Deutzmann, R.3    Trüper, H.G.4
  • 18
    • 0027239614 scopus 로고
    • The ferredoxin; sulphite reductase gene from Synechococcus PCC7942
    • 1B. Gisselmann G, Klausmeier P, Schwenn JD: The ferredoxin; sulphite reductase gene from Synechococcus PCC7942. Biochim Biophys Acta 1993, 1144:102-106.
    • (1993) Biochim Biophys Acta , vol.1144 , pp. 102-106
    • Gisselmann, G.1    Klausmeier, P.2    Schwenn, J.D.3
  • 19
    • 0027564467 scopus 로고
    • Nitrite reductase gene from Synechococcus sp. PCC 7942: Homology between cyanobacterial and higher-plant nitrite reductases
    • 19. Luque I, Flores E, Herrero A: Nitrite reductase gene from Synechococcus sp. PCC 7942: homology between cyanobacterial and higher-plant nitrite reductases. Plant Mol Biol 1993, 21:1201-1205.
    • (1993) Plant Mol Biol , vol.21 , pp. 1201-1205
    • Luque, I.1    Flores, E.2    Herrero, A.3
  • 20
    • 0025942475 scopus 로고
    • Primary structure of the assimilatory-type sulfite reductase from Desulfovibrio vulgaris (Hildenborough): Cloning and nucleotide sequence of the reductase gene
    • 20. Tan J, Helms LR, Swenson RP, Cowan JA: Primary structure of the assimilatory-type sulfite reductase from Desulfovibrio vulgaris (Hildenborough): cloning and nucleotide sequence of the reductase gene. Biochemistry 1991, 30:9900-9907.
    • (1991) Biochemistry , vol.30 , pp. 9900-9907
    • Tan, J.1    Helms, L.R.2    Swenson, R.P.3    Cowan, J.A.4
  • 21
    • 0015983758 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria 3. The Escherichia coli hemoflavoprotein: Catalytic parameters and the sequence of electron flow
    • 21. Siegel LM, Davis PS, Kamin H: Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow. J Biol Chem 1974, 249:1572-1586.
    • (1974) J Biol Chem , vol.249 , pp. 1572-1586
    • Siegel, L.M.1    Davis, P.S.2    Kamin, H.3
  • 22
    • 0015968302 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 4. The Escherichia coli hemoflavoprotein: Subunit structure and dissociation into hemoprotein and flavoprotein components
    • 22. Siegel LM, Davis PS: Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 4. The Escherichia coli hemoflavoprotein: subunit structure and dissociation into hemoprotein and flavoprotein components. J Biol Chem 1974, 249:1587-1598.
    • (1974) J Biol Chem , vol.249 , pp. 1587-1598
    • Siegel, L.M.1    Davis, P.S.2
  • 23
    • 0019977937 scopus 로고
    • Escherichia coli sulfite reductase hemoprotein subunit-prosthetic groups, catalytic parameters and ligand complexes
    • 23. Siegel LM, Rueger DC, Barber MJ, Krueger RJ, Orme-Johnson NR, Orme-Johnson WH: Escherichia coli sulfite reductase hemoprotein subunit-prosthetic groups, catalytic parameters and ligand complexes. J Biol Chem 1982, 257:6343-6350.
    • (1982) J Biol Chem , vol.257 , pp. 6343-6350
    • Siegel, L.M.1    Rueger, D.C.2    Barber, M.J.3    Krueger, R.J.4    Orme-Johnson, N.R.5    Orme-Johnson, W.H.6
  • 25
    • 0027433508 scopus 로고
    • The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metallated sirohemes and S =9/2 iron-sulfur clusters
    • 25. Arendsen AF, Verhagen MFJM, Wolbert RBG, Pierik AJ, Stams AJM, Jetten MSM, Hagen WR: The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metallated sirohemes and S =9/2 iron-sulfur clusters. Biochemistry 1993, 32:10323-10330.
    • (1993) Biochemistry , vol.32 , pp. 10323-10330
    • Arendsen, A.F.1    Verhagen, M.F.J.M.2    Wolbert, R.B.G.3    Pierik, A.J.4    Stams, A.J.M.5    Jetten, M.S.M.6    Hagen, W.R.7
  • 26
    • 0028845796 scopus 로고
    • Molecular properties of the dissimilatory sulfite reductase from Desulfovibrio desulfuricans (Essex) and comparison with the enzyme from Desulfovibrio vulgaris (Hildenborough)
    • 26. Steuber J, Arendsen AF, Hagen WR, Kroneck PM: Molecular properties of the dissimilatory sulfite reductase from Desulfovibrio desulfuricans (Essex) and comparison with the enzyme from Desulfovibrio vulgaris (Hildenborough). Eur J Biochem 1995, 223:873-879. Two forms of D. desulfuricans desulfoviridin are isolated and found to have iron compositions and spectroscopic characteristics quite different from those reported for the D. vulgaris desulfoviridin [30].
    • (1995) Eur J Biochem , vol.223 , pp. 873-879
    • Steuber, J.1    Arendsen, A.F.2    Hagen, W.R.3    Kroneck, P.M.4
  • 27
    • 0027469586 scopus 로고
    • Expression of the γ-subunit of desulfoviridin-type dissimilatory sulfite reductase and of the α- and β-subunit genes is not coordinately regulated
    • 27. Karkhoff Schweizer RR, Bruschi M, Voordouw G: Expression of the γ-subunit of desulfoviridin-type dissimilatory sulfite reductase and of the α- and β-subunit genes is not coordinately regulated. Eur J Biochem 1993, 211:501-507.
    • (1993) Eur J Biochem , vol.211 , pp. 501-507
    • Karkhoff Schweizer, R.R.1    Bruschi, M.2    Voordouw, G.3
  • 28
    • 0023870575 scopus 로고
    • Characterization of two dissimilatory sulfite reductases (Desulforubidin and Desulfoviridin) from the sulfate-reducing bacteria. Mössbauer and EPR studies
    • 28. Moura I, LeGall J, Lino AR, Peck HD Jr, Fauque G, Xavier AV, DerVartanian DV. Moura JJG, Huynh BH: Characterization of two dissimilatory sulfite reductases (Desulforubidin and Desulfoviridin) from the sulfate-reducing bacteria. Mössbauer and EPR studies. J Am Chem Soc 1988, 110:1075-1082.
    • (1988) J Am Chem Soc , vol.110 , pp. 1075-1082
    • Moura, I.1    LeGall, J.2    Lino, A.R.3    Peck H.D., Jr.4    Fauque, G.5    Xavier, A.V.6    DerVartanian, D.V.7    Moura, J.J.G.8    Huynh, B.H.9
  • 29
    • 0025351899 scopus 로고
    • Purification and characterization of bisulfite reductase (desulfofuscidin) from Desulfovibrio thermophilus and its complexes with exogenous ligands
    • 29. Fauque G, Lino AR, Czechowski M, Kang L, DerVartanian DV, Moura JJG, LeGall J, Moura I: Purification and characterization of bisulfite reductase (desulfofuscidin) from Desulfovibrio thermophilus and its complexes with exogenous ligands. Biochim Biophys Acta 1990, 1040:112-118.
    • (1990) Biochim Biophys Acta , vol.1040 , pp. 112-118
    • Fauque, G.1    Lino, A.R.2    Czechowski, M.3    Kang, L.4    DerVartanian, D.V.5    Moura, J.J.G.6    LeGall, J.7    Moura, I.8
  • 30
    • 0028214186 scopus 로고
    • Desulfoviridin: A multimeric-dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Purification, characterization, kinetics and EPR studies
    • 30. Wolfe BM, Lui SM, Cowan JA: Desulfoviridin: a multimeric-dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Purification, characterization, kinetics and EPR studies. Eur J Biochem 1994, 223:79-89.
    • (1994) Eur J Biochem , vol.223 , pp. 79-89
    • Wolfe, B.M.1    Lui, S.M.2    Cowan, J.A.3
  • 31
    • 0025971461 scopus 로고
    • S=9/2 EPR signals are evidence against coupling between the siroheme and the Fe/S prosthetic groups in Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase
    • 31. Pierik AJ, Hagen WJ: S=9/2 EPR signals are evidence against coupling between the siroheme and the Fe/S prosthetic groups in Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase. Eur J Biochem 1991, 195:505-516.
    • (1991) Eur J Biochem , vol.195 , pp. 505-516
    • Pierik, A.J.1    Hagen, W.J.2
  • 32
    • 0020409892 scopus 로고
    • 4 prosthetic groups in Escherichia coli sulfite reductase hemoprotein subunit
    • 4 prosthetic groups in Escherichia coli sulfite reductase hemoprotein subunit. Biochemistry 1982, 21:3538-3547.
    • (1982) Biochemistry , vol.21 , pp. 3538-3547
    • Janick, P.1    Siegel, L.M.2
  • 33
    • 0020477453 scopus 로고
    • Spinach siroheme enzymes: Isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferredoxin-nitrite reductase
    • 33. Krueger RJ, Siegel LM: Spinach siroheme enzymes: isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferredoxin-nitrite reductase. Biochemistry 1982, 21:2892-2904.
    • (1982) Biochemistry , vol.21 , pp. 2892-2904
    • Krueger, R.J.1    Siegel, L.M.2
  • 34
    • 0021112592 scopus 로고
    • Mössbauer evidence for exchanged-coupled siroheme and [4Fe-4S] prosthetic groups in Escherichia coli sulfite reductase -studies of the reduced states and of a nitrite turnover complex
    • 34. Christner JA, Münck. E, Janick PA, Siegel LM: Mössbauer evidence for exchanged-coupled siroheme and [4Fe-4S] prosthetic groups in Escherichia coli sulfite reductase -studies of the reduced states and of a nitrite turnover complex. J Biol Chem 1983, 258:11147-11156.
    • (1983) J Biol Chem , vol.258 , pp. 11147-11156
    • Christner, J.A.1    Münck, E.2    Janick, P.A.3    Siegel, L.M.4
  • 35
    • 0021723164 scopus 로고
    • Exchange coupling between siroheme and [4Fe-4S] cluster in E. coli sulfite reductase. Mössbauer studies and coupling models for a 2-electron reduced enzyme state and complexes with sulfide
    • 35. Christner JA, Münck E, Kent TA, Janick PA, Salerno JC, Siegel LM: Exchange coupling between siroheme and [4Fe-4S] cluster in E. coli sulfite reductase. Mössbauer studies and coupling models for a 2-electron reduced enzyme state and complexes with sulfide. J Am Chem Soc 1984, 106:6786-6794.
    • (1984) J Am Chem Soc , vol.106 , pp. 6786-6794
    • Christner, J.A.1    Münck, E.2    Kent, T.A.3    Janick, P.A.4    Salerno, J.C.5    Siegel, L.M.6
  • 36
    • 0021747975 scopus 로고
    • Characterization of a sulfite reductase from Desulfovibrio vulgaris - Evidence for the presence of a low-spin siroheme and an exchange-coupled siroheme-[4Fe-4S] unit
    • 36. Huynh BH, Kang L, DerVartanian DV, Peck HD Jr, LeGall J: Characterization of a sulfite reductase from Desulfovibrio vulgaris - evidence for the presence of a low-spin siroheme and an exchange-coupled siroheme-[4Fe-4S] unit J Biol Chem 1984, 259:15373-15376.
    • (1984) J Biol Chem , vol.259 , pp. 15373-15376
    • Huynh, B.H.1    Kang, L.2    DerVartanian, D.V.3    Peck H.D., Jr.4    LeGall, J.5
  • 38
    • 0024389516 scopus 로고
    • Resonance raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes
    • 38. Han S, Madden JF, Thompson RG, Strauss SH, Siegel LM, Spiro TG: Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes. Biochemistry 1989, 28:5461-5471.
    • (1989) Biochemistry , vol.28 , pp. 5461-5471
    • Han, S.1    Madden, J.F.2    Thompson, R.G.3    Strauss, S.H.4    Siegel, L.M.5    Spiro, T.G.6
  • 39
    • 0027521058 scopus 로고
    • Proton NMR of Escherichia coli sulfite reductase: The unligated hemoprotein subunit
    • 39. Kaufman J, Spicer LD, Siegel LM: Proton NMR of Escherichia coli sulfite reductase: the unligated hemoprotein subunit. Biochemistry 1993, 32:2853-2867.
    • (1993) Biochemistry , vol.32 , pp. 2853-2867
    • Kaufman, J.1    Spicer, L.D.2    Siegel, L.M.3
  • 41
    • 21344469078 scopus 로고
    • 4-Fe active site of sulfite reductase
    • 4-Fe active site of sulfite reductase. Chem Phys 1995, 201:343-356.
    • (1995) Chem Phys , vol.201 , pp. 343-356
    • Belinsky, M.I.1
  • 42
    • 0030099771 scopus 로고    scopus 로고
    • 4-Fe] active site of Escherichia coli sulfite reductase
    • 1H NMR experiments, and its seemingly diamagnetic state as seen by EPR and magnetic experiments.
    • (1996) Chem Phys Lett , vol.250 , pp. 320-327
    • Belinsky, M.I.1
  • 44
    • 0030985155 scopus 로고    scopus 로고
    • Determining phases and anomalous scattering models from the multiwavelength diffraction of native protein metal clusters. Improved mad phase error estimates and anomalous scatterer positions
    • in press
    • 44. Crane BR, Getzoff ED: Determining phases and anomalous scattering models from the multiwavelength diffraction of native protein metal clusters. Improved MAD phase error estimates and anomalous scatterer positions. Acta Crystallogr D 1997, 53:in press.
    • (1997) Acta Crystallogr D , vol.53
    • Crane, B.R.1    Getzoff, E.D.2
  • 45
    • 0028071502 scopus 로고
    • Functional expression and characterization of the assimilatory-type sulfite reductase from Desulfovibrio vulgaris (Hildenborough)
    • 45. Tan J, Soriano A, Lui SM, Cowan JA: Functional expression and characterization of the assimilatory-type sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Arch Biochem Biophys 1994, 312:516-523.
    • (1994) Arch Biochem Biophys , vol.312 , pp. 516-523
    • Tan, J.1    Soriano, A.2    Lui, S.M.3    Cowan, J.A.4
  • 46
    • 0011309055 scopus 로고    scopus 로고
    • Optical and EPR characterization of Desulfovibrio (Hildenborough) sulfite reductase and ligand adducts
    • 46. Lui SM, Cowan JA: Optical and EPR characterization of Desulfovibrio (Hildenborough) sulfite reductase and ligand adducts. Inorg Chim Acta 1996, 242:25-30.
    • (1996) Inorg Chim Acta , vol.242 , pp. 25-30
    • Lui, S.M.1    Cowan, J.A.2
  • 47
    • 0025883965 scopus 로고
    • 2- by the assimilatory-type sulfite reductase from Desulfovibrio vulgaris (Hildenborough)
    • 2- by the assimilatory-type sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Biochemistry 1991, 30:8910-8917.
    • (1991) Biochemistry , vol.30 , pp. 8910-8917
    • Tan, J.1    Cowan, J.A.2
  • 48
    • 0004681868 scopus 로고
    • 4-S-Fe(III)] bridged assemblies related to the exchange-coupled catalytic site of sulfite reductases
    • 4-S-Fe(III)] bridged assemblies related to the exchange-coupled catalytic site of sulfite reductases. J Am Chem Soc 1994, 71:7177-7188.
    • (1994) J Am Chem Soc , vol.71 , pp. 7177-7188
    • Cai, L.1    Holm, R.H.2
  • 50
    • 0000782682 scopus 로고    scopus 로고
    • 4-S-Fe(III) bridged assembly containing an isobacteriochlorin component: A further analogue of the active site of sulfite reductase
    • 1H-NMR spectra of the cluster ligand system that occur when two isobacteriochlorin diasteriomers are present.
    • (1996) Inorg Chem , vol.35 , pp. 2767-2772
    • Cai, L.1    Holm, R.H.2
  • 51
    • 11944257212 scopus 로고
    • Interplay of electron exchange and electron transfer in metal polynuclear complexes in proteins and chemical models
    • 51. Blondin G, Girerd J: Interplay of electron exchange and electron transfer in metal polynuclear complexes in proteins and chemical models. Chem Rev 1990, 90:1359-1376.
    • (1990) Chem Rev , vol.90 , pp. 1359-1376
    • Blondin, G.1    Girerd, J.2
  • 52
    • 32544433641 scopus 로고
    • Density-functional theory of spin polarization and spin coupling in iron-sulfur clusters
    • 52. Noodleman L, Case DA: Density-functional theory of spin polarization and spin coupling in iron-sulfur clusters. Adv Inorg Chem 1992, 38:423-469.
    • (1992) Adv Inorg Chem , vol.38 , pp. 423-469
    • Noodleman, L.1    Case, D.A.2
  • 53
    • 0028257466 scopus 로고
    • Direct reversible protein electrochemistry at a pyrolytic graphite electrode
    • 4]-sirohaem prosthetic center in the hexameric dissimilatory sulfite reductase and the monomeric assimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Systematic pH titration experiments and implications for active-site chemistry
    • 4]-sirohaem prosthetic center in the hexameric dissimilatory sulfite reductase and the monomeric assimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Systematic pH titration experiments and implications for active-site chemistry. J Am Chem Soc 1994, 116:11538-11549.
    • (1994) J Am Chem Soc , vol.116 , pp. 11538-11549
    • Lui, S.M.1    Cowan, J.A.2
  • 56
    • 0028880656 scopus 로고
    • Expression of spinach nitrite reductase in E. coli: Site-directed mutagenesis of predicted active site amino acids
    • 56. Bellissimo DB, Privalle LS: Expression of spinach nitrite reductase in E. coli: site-directed mutagenesis of predicted active site amino acids. Arch Biochem Biophys 1995, 323:155-163. Site-directed mutagenesis experiments on the spinach NiR indicate that few changes of the residues surrounding the cluster ligands can be structurally tolerated. One mutant, Glu513Ala, produced a functional protein with a decreased catalytic activity and an altered optical spectrum.
    • (1995) Arch Biochem Biophys , vol.323 , pp. 155-163
    • Bellissimo, D.B.1    Privalle, L.S.2
  • 57
    • 0020702316 scopus 로고
    • Characterization of complexes between Escherichia coli sulfite reductase hemoprotein subunit and its substrates sulfite and nitrite
    • 57. Janick PA, Rueger DC, Krueger RJ, Barber MJ, Siegel LM: Characterization of complexes between Escherichia coli sulfite reductase hemoprotein subunit and its substrates sulfite and nitrite. Biochemistry 1983, 22:396-408.
    • (1983) Biochemistry , vol.22 , pp. 396-408
    • Janick, P.A.1    Rueger, D.C.2    Krueger, R.J.3    Barber, M.J.4    Siegel, L.M.5
  • 58
    • 0028038311 scopus 로고
    • Conformational gating of the dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Synthesis, characterization, and stopped-flow kinetics studies of 1,5-IEDANS-labeled desulfovirdin
    • 58. Lui SM, Cowan JA: Conformational gating of the dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). synthesis, characterization, and stopped-flow kinetics studies of 1,5-IEDANS-labeled desulfovirdin. Biochemistry 1994, 33:11209-11216.
    • (1994) Biochemistry , vol.33 , pp. 11209-11216
    • Lui, S.M.1    Cowan, J.A.2
  • 59
    • 0023812965 scopus 로고
    • Activated conformers of Escherichia coli sulfite reductase heme protein subunit
    • 59. Young LJ, Siegel LM: Activated conformers of Escherichia coli sulfite reductase heme protein subunit. Biochemistry 1988, 27:4991-4999.
    • (1988) Biochemistry , vol.27 , pp. 4991-4999
    • Young, L.J.1    Siegel, L.M.2
  • 60
    • 0011352431 scopus 로고
    • Analysis of a siroheme model compound: Core-size dependence of resonance raman bands and the siroheme spin state in sulfite reductase
    • 60. Melamed D, Sullivan EPS Jr, Prendergast K, Strauss SH, Spiro TG: Analysis of a siroheme model compound: core-size dependence of resonance Raman bands and the siroheme spin state in sulfite reductase. Inorg Chem 1991, 30:1308-1319.
    • (1991) Inorg Chem , vol.30 , pp. 1308-1319
    • Melamed, D.1    Sullivan E.P.S., Jr.2    Prendergast, K.3    Strauss, S.H.4    Spiro, T.G.5
  • 61
    • 0027326473 scopus 로고
    • Resonance raman study of sirohydrochlorin and siroheme in sulfite reductases from sulfate reducing bacteria
    • 61. Underwood-Lemons T, Moura I, Yue KT: Resonance Raman study of sirohydrochlorin and siroheme in sulfite reductases from sulfate reducing bacteria. Biochim Biophys Acta 1993, 1157:275-284.
    • (1993) Biochim Biophys Acta , vol.1157 , pp. 275-284
    • Underwood-Lemons, T.1    Moura, I.2    Yue, K.T.3
  • 62
    • 0011268993 scopus 로고
    • 4-siroheme of the assimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough)
    • 4-siroheme of the assimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). Inorg Chem 1990, 29:2176-2179.
    • (1990) Inorg Chem , vol.29 , pp. 2176-2179
    • Cowan, J.1    Sola, M.2
  • 63
    • 0001512163 scopus 로고
    • Enzymatic reduction of inorganic anions. Pre-steady-state kinetic analysis of the dissimitatory sulfite reductase (Desulfoviridin) from Desulfovibrio vulgaris (Hildenborough). Mechanistic implications
    • 63. Lui SM, Soriano A, Cowan JA: Enzymatic reduction of inorganic anions. Pre-steady-state kinetic analysis of the dissimitatory sulfite reductase (Desulfoviridin) from Desulfovibrio vulgaris (Hildenborough). Mechanistic implications. J Am Chem Soc 1993, 115:10483-10485.
    • (1993) J Am Chem Soc , vol.115 , pp. 10483-10485
    • Lui, S.M.1    Soriano, A.2    Cowan, J.A.3
  • 64
    • 0002511312 scopus 로고
    • Structure and function of spinach ferredoxin-nitrite reductase
    • Edited by Wray JA, Kingham JR. Oxford: Oxford Science Publications
    • 64. Siegel LM, Wilkerson JO: Structure and function of spinach ferredoxin-nitrite reductase. In Molecular and Genetic Aspects of Nitrate Assimilation. Edited by Wray JA, Kingham JR. Oxford: Oxford Science Publications; 1989:263-283.
    • (1989) Molecular and Genetic Aspects of Nitrate Assimilation , pp. 263-283
    • Siegel, L.M.1    Wilkerson, J.O.2
  • 65
    • 0015992799 scopus 로고
    • Redox potentials of certain vitamins. K: Implications for a role in sulfite reduction by obligately anaerobic bacteria
    • 65. Wagner GC, Kassner RJ, Kamen MD: Redox potentials of certain vitamins. K: implications for a role in sulfite reduction by obligately anaerobic bacteria. Proc Natl Acad Sci USA 1974, 71:253-256.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 253-256
    • Wagner, G.C.1    Kassner, R.J.2    Kamen, M.D.3
  • 66
    • 0028002027 scopus 로고
    • Enzymatic reduction of inorganic anions. Variable-temperature steady-state and pre-steady-state kinetics experiments to map the energy profile of an enzymatic multielectron redox reaction. Application to the dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough)
    • 66. Lui SM, Liang W, Soriano A, Cowan JA: Enzymatic reduction of inorganic anions. Variable-temperature steady-state and pre-steady-state kinetics experiments to map the energy profile of an enzymatic multielectron redox reaction. Application to the dissimilatory sulfite reductase from Desulfovibrio vulgaris (Hildenborough). J Am Chem Soc 1994, 116:4531-4536.
    • (1994) J Am Chem Soc , vol.116 , pp. 4531-4536
    • Lui, S.M.1    Liang, W.2    Soriano, A.3    Cowan, J.A.4
  • 67
    • 0024294403 scopus 로고
    • Probing structure-function relationships in heme-containing oxygenases and peroxidases
    • 67 Dawson JH: Probing structure-function relationships in heme-containing oxygenases and peroxidases. Science 1988, 240:1308-1319.
    • (1988) Science , vol.240 , pp. 1308-1319
    • Dawson, J.H.1
  • 68
    • 0023810222 scopus 로고
    • Heme enzyme crystal structures
    • 68. Poulos TL: Heme enzyme crystal structures. Adv Inorg Biochem 1988, 7:1-36.
    • (1988) Adv Inorg Biochem , vol.7 , pp. 1-36
    • Poulos, T.L.1
  • 69
    • 0003450383 scopus 로고
    • New York: The Ronald Press Company
    • 69. Price CC, Oae S: Sulfur Bonding. New York: The Ronald Press Company; 1962.
    • (1962) Sulfur Bonding
    • Price, C.C.1    Oae, S.2
  • 71
    • 0024354883 scopus 로고
    • Resonance raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes
    • 71. Han S, Madden JF, Siegel LM, Spiro TG: Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes. Biochemistry 1989, 26:5477-5485.
    • (1989) Biochemistry , vol.26 , pp. 5477-5485
    • Han, S.1    Madden, J.F.2    Siegel, L.M.3    Spiro, T.G.4
  • 72
    • 0040488939 scopus 로고
    • 4]-siroheme prosthetic center of a dissimilatory sulfite reductase
    • 4]-siroheme prosthetic center of a dissimilatory sulfite reductase. Inorg Chem 1994, 33:4504-4606.
    • (1994) Inorg Chem , vol.33 , pp. 4504-4606
    • Liang, W.1    Cowan, J.A.2
  • 74
    • 0015907498 scopus 로고
    • Siroheme and sirohydrochlorin -the basis for a new type of porphyrin-related prosthetic group common to both assimilatory and dissimilatory sulfite reductases
    • 74. Murphy MJ, Siegel LM: Siroheme and sirohydrochlorin -the basis for a new type of porphyrin-related prosthetic group common to both assimilatory and dissimilatory sulfite reductases. J Biol Chem 1973, 248:6911-6919.
    • (1973) J Biol Chem , vol.248 , pp. 6911-6919
    • Murphy, M.J.1    Siegel, L.M.2
  • 75
    • 0001029544 scopus 로고
    • Siroheme: A new prosthetic group participating in six-electron reduction reactions catalyzed by both sulfite and nitrite reductases
    • 75. Murphy MJ, Siegel LM, Tove SR, Kamin H: Siroheme: a new prosthetic group participating in six-electron reduction reactions catalyzed by both sulfite and nitrite reductases. Proc Nat Acad Sci USA 1974, 71:612-616.
    • (1974) Proc Nat Acad Sci USA , vol.71 , pp. 612-616
    • Murphy, M.J.1    Siegel, L.M.2    Tove, S.R.3    Kamin, H.4
  • 76
    • 0023159558 scopus 로고
    • Isolation of extremely thermophilic sulfate reducers: Evidence for a novel branch of archaebacteria
    • 76. Stetter KO, Lauerer G, Thomm M, Neuner A: Isolation of extremely thermophilic sulfate reducers: evidence for a novel branch of Archaebacteria. Science 1987, 236:822-824.
    • (1987) Science , vol.236 , pp. 822-824
    • Stetter, K.O.1    Lauerer, G.2    Thomm, M.3    Neuner, A.4
  • 77
    • 0002308927 scopus 로고
    • Isotopic inferences of ancient biochemistries: Carbon, sulfur, hydrogen, and nitrogen
    • Princeton: Princeton University Press
    • 77 Schidlowski M, Hayes JM, Kaplan IR: Isotopic inferences of ancient biochemistries: carbon, sulfur, hydrogen, and nitrogen. In Earth's Earliest Biosphere, Its Origin and Evolution. Princeton: Princeton University Press; 1983:149-186.
    • (1983) Earth's Earliest Biosphere, Its Origin and Evolution , pp. 149-186
    • Schidlowski, M.1    Hayes, J.M.2    Kaplan, I.R.3
  • 78
    • 0019999193 scopus 로고
    • Sulphate and sulphate reduction in early Precambrian oceans
    • 78. Cameron EM: Sulphate and sulphate reduction in early Precambrian oceans. Nature 1982, 296:145-148.
    • (1982) Nature , vol.296 , pp. 145-148
    • Cameron, E.M.1
  • 80
    • 0023727338 scopus 로고
    • Superoxidized states of Escherichia coli sulfite reductase heme protein subunit
    • 80. Young LJ, Siegel LM: Superoxidized states of Escherichia coli sulfite reductase heme protein subunit. Biochemistry 1988, 27:5984-5990.
    • (1988) Biochemistry , vol.27 , pp. 5984-5990
    • Young, L.J.1    Siegel, L.M.2
  • 81
    • 33845551753 scopus 로고
    • Models for nitrite reductases. Redox chemistry of iron nitrosyl porphyrins, chlorins, and isobacteriochlorins and π-cation radicals of cobalt nitrosyl isobacteriochlorins
    • 81. Fujita E, Fajer J: Models for nitrite reductases. Redox chemistry of iron nitrosyl porphyrins, chlorins, and isobacteriochlorins and π-cation radicals of cobalt nitrosyl isobacteriochlorins. J Am Chem Soc 1983, 105:6743-6745.
    • (1983) J Am Chem Soc , vol.105 , pp. 6743-6745
    • Fujita, E.1    Fajer, J.2
  • 82
    • 33847087690 scopus 로고
    • Models for siroheme and sirohydrochlorin. π-cation radicals of iron(II) isobacteriochlorin
    • 82. Chang CK, Fajer J: Models for siroheme and sirohydrochlorin. π-cation radicals of iron(II) isobacteriochlorin. J Am Chem Soc 1980, 102:848-851.
    • (1980) J Am Chem Soc , vol.102 , pp. 848-851
    • Chang, C.K.1    Fajer, J.2
  • 83
    • 0002322140 scopus 로고
    • The electrochemical reduction of iron porphyrin nitrosyls in the presence of weak acids
    • 83. Liu Y, Ryan MD: The electrochemical reduction of iron porphyrin nitrosyls in the presence of weak acids. J Electroanal Chem 1994, 368:209-219.
    • (1994) J Electroanal Chem , vol.368 , pp. 209-219
    • Liu, Y.1    Ryan, M.D.2
  • 84
    • 0023391016 scopus 로고
    • Spectroscopic properties of siroheme extracted from sulfite reductases
    • 84. Kang L, LeGall J, Kowal AT, Johnson MK: Spectroscopic properties of siroheme extracted from sulfite reductases. J Inorg Biochem 1987, 30:273-290.
    • (1987) J Inorg Biochem , vol.30 , pp. 273-290
    • Kang, L.1    LeGall, J.2    Kowal, A.T.3    Johnson, M.K.4
  • 85
    • 0029158963 scopus 로고
    • Sulfite reductase: Active site residues are noncatalytic. Comparison of reaction energetics for enzyme- and siroheme-catalyzed reduction of inorganic substrates
    • 85. Soriano A, Cowan JA: Sulfite reductase: active site residues are noncatalytic. Comparison of reaction energetics for enzyme- and siroheme-catalyzed reduction of inorganic substrates. J Am Chem Soc 1995, 117:4724-4725. Steady-state kinetic parameters derived for the reduction of sulfite, nitrite and hydroxylamine by free siroheme and the dSiR and alSiR from D. vulgaris indicate that free siroheme in the presence of substrate can consume reductant as well as, or better than the enzymes: however, the products generated are not characterized. A mechanism is presented for sulfite reduction by free siroheme with uncompetitive inhibition by trithionate.
    • (1995) J Am Chem Soc , vol.117 , pp. 4724-4725
    • Soriano, A.1    Cowan, J.A.2
  • 86
    • 0028673777 scopus 로고
    • Desulforubidin: Dissimilatory, high-spin sulfite reductase of Desulfomicrobium species
    • 86. DerVartanian DV: Desulforubidin: dissimilatory, high-spin sulfite reductase of Desulfomicrobium species. Methods Enzymol 1994, 243:270-276.
    • (1994) Methods Enzymol , vol.243 , pp. 270-276
    • DerVartanian, D.V.1
  • 87
    • 0014868152 scopus 로고
    • Carbon monoxide-reacting pigment from Desulfotomaculum nigrificans and its possible relevance to sulfite reduction
    • 87. Trudinger PA: Carbon monoxide-reacting pigment from Desulfotomaculum nigrificans and its possible relevance to sulfite reduction. J Bacteriol 1970, 104:158-170.
    • (1970) J Bacteriol , vol.104 , pp. 158-170
    • Trudinger, P.A.1
  • 88
    • 0028673419 scopus 로고
    • Desulfofuscidin: Dissimilatory, high-spin sulfite reductase of thermophilic sulfate-reducing bacteria
    • 88. Hatchikian EC: Desulfofuscidin: dissimilatory, high-spin sulfite reductase of thermophilic sulfate-reducing bacteria. Methods Enzymol 1994, 243:276-295.
    • (1994) Methods Enzymol , vol.243 , pp. 276-295
    • Hatchikian, E.C.1
  • 89
    • 0028673855 scopus 로고
    • Reverse siroheme sulfite reductase from Thiobacillus denitrificans
    • 89. Trüper HG: Reverse siroheme sulfite reductase from Thiobacillus denitrificans. Methods Enzymol 1994, 243:270-276.
    • (1994) Methods Enzymol , vol.243 , pp. 270-276
    • Trüper, H.G.1
  • 90
    • 0028672762 scopus 로고
    • Low-spin sulfite reductases
    • 90. Moura I, Lino AR: Low-spin sulfite reductases. Methods Enzymol 1994, 243:296-303.
    • (1994) Methods Enzymol , vol.243 , pp. 296-303
    • Moura, I.1    Lino, A.R.2
  • 91
    • 0024430827 scopus 로고
    • Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli
    • 91. Ostrowski J, Wu J, Rueger DC, Miller BE, Siegel LM, Kredich NM: Characterization of the cysJIH Regions of Salmonella typhimurium and Escherichia coli. J Biol Chem 1989, 264:15726-15737.
    • (1989) J Biol Chem , vol.264 , pp. 15726-15737
    • Ostrowski, J.1    Wu, J.2    Rueger, D.C.3    Miller, B.E.4    Siegel, L.M.5    Kredich, N.M.6
  • 92
    • 0023989829 scopus 로고
    • Isolation of cDNA clones coding for spinach nitrite reductase: Complete sequence and nitrate induction
    • 92. Back E, Burkhart W, Moyer M, Privalle L, Rothstein S: Isolation of cDNA clones coding for spinach nitrite reductase: complete sequence and nitrate induction. Mol Gen Genet 1988, 212:20-26.
    • (1988) Mol Gen Genet , vol.212 , pp. 20-26
    • Back, E.1    Burkhart, W.2    Moyer, M.3    Privalle, L.4    Rothstein, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.